{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,1,28]],"date-time":"2026-01-28T03:05:21Z","timestamp":1769569521294,"version":"3.49.0"},"reference-count":56,"publisher":"American Society for Microbiology","issue":"11","license":[{"start":{"date-parts":[[2015,6,1]],"date-time":"2015-06-01T00:00:00Z","timestamp":1433116800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["J Bacteriol"],"published-print":{"date-parts":[[2015,6]]},"abstract":"ABSTRACT<\/jats:title>\n \n d<\/jats:sc>\n -Glutamate is an essential component of bacterial peptidoglycan and a building block of the poly-\u03b3-\n d<\/jats:sc>\n -glutamic acid (PDGA) capsule of\n Bacillus anthracis<\/jats:named-content>\n , the causative agent of anthrax. Earlier work suggested that two glutamate racemases, encoded by\n racE1<\/jats:italic>\n and\n racE2<\/jats:italic>\n , are each essential for growth of\n B. anthracis<\/jats:named-content>\n , supplying\n d<\/jats:sc>\n -glutamic acid for the synthesis of peptidoglycan and PDGA capsule. Earlier work could not explain, however, why two enzymes that catalyze the same reaction may be needed for bacterial growth. Here, we report that deletion of\n racE1<\/jats:italic>\n or\n racE2<\/jats:italic>\n did not prevent growth of\n B. anthracis<\/jats:named-content>\n Sterne (pXO1\n +<\/jats:sup>\n pXO2\n \u2212<\/jats:sup>\n ), the noncapsulating vaccine strain, or of\n B. anthracis<\/jats:named-content>\n Ames (pXO1\n +<\/jats:sup>\n pXO2\n +<\/jats:sup>\n ), a fully virulent, capsulating isolate. While mutants with deletions in\n racE1<\/jats:italic>\n and\n racE2<\/jats:italic>\n were not viable,\n racE2<\/jats:italic>\n deletion delayed vegetative growth of\n B. anthracis<\/jats:named-content>\n following spore germination and caused aberrant cell shapes, phenotypes that were partially restored by exogenous\n d<\/jats:sc>\n -glutamate. Deletion of\n racE1<\/jats:italic>\n or\n racE2<\/jats:italic>\n from\n B. anthracis<\/jats:named-content>\n Ames did not affect the production or stereochemical composition of the PDGA capsule. A model is presented whereby\n B. anthracis<\/jats:named-content>\n , similar to\n Bacillus subtilis<\/jats:named-content>\n , utilizes two functionally redundant racemase enzymes to synthesize\n d<\/jats:sc>\n -glutamic acid for peptidoglycan synthesis.\n <\/jats:p>\n \n IMPORTANCE<\/jats:bold>\n Glutamate racemases, enzymes that convert\n l<\/jats:sc>\n -glutamate to\n d<\/jats:sc>\n -glutamate, are targeted for antibiotic development. Glutamate racemase inhibitors may be useful for the treatment of bacterial infections such as anthrax, where the causative agent,\n B. anthracis<\/jats:named-content>\n , requires\n d<\/jats:sc>\n -glutamate for the synthesis of peptidoglycan and poly-\u03b3-\n d<\/jats:sc>\n -glutamic acid (PDGA) capsule. Here we show that\n B. anthracis<\/jats:named-content>\n possesses two glutamate racemase genes that can be deleted without abolishing either bacterial growth or PDGA synthesis. These data indicate that drug candidates must inhibit both glutamate racemases, RacE1 and RacE2, in order to block\n B. anthracis<\/jats:named-content>\n growth and achieve therapeutic efficacy.\n <\/jats:p>","DOI":"10.1128\/jb.00070-15","type":"journal-article","created":{"date-parts":[[2015,3,17]],"date-time":"2015-03-17T02:13:00Z","timestamp":1426558380000},"page":"1854-1861","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":16,"title":["Glutamate Racemase Mutants of Bacillus anthracis"],"prefix":"10.1128","volume":"197","author":[{"given":"So-Young","family":"Oh","sequence":"first","affiliation":[{"name":"Howard Taylor Ricketts Laboratory, Argonne National Laboratory, Lemont, Illinois, USA"},{"name":"Department of Microbiology, University of Chicago, Chicago, Illinois, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Stefan G.","family":"Richter","sequence":"additional","affiliation":[{"name":"Howard Taylor Ricketts Laboratory, Argonne National Laboratory, Lemont, Illinois, USA"},{"name":"Department of Microbiology, University of Chicago, Chicago, Illinois, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Dominique M.","family":"Missiakas","sequence":"additional","affiliation":[{"name":"Howard Taylor Ricketts Laboratory, Argonne National Laboratory, Lemont, Illinois, USA"},{"name":"Department of Microbiology, University of Chicago, Chicago, Illinois, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Olaf","family":"Schneewind","sequence":"additional","affiliation":[{"name":"Howard Taylor Ricketts Laboratory, Argonne National Laboratory, Lemont, Illinois, USA"},{"name":"Department of Microbiology, University of Chicago, Chicago, Illinois, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"235","reference":[{"key":"e_1_3_2_2_2","doi-asserted-by":"publisher","DOI":"10.1128\/jb.114.2.499-506.1973"},{"key":"e_1_3_2_3_2","doi-asserted-by":"publisher","DOI":"10.1146\/annurev-biochem-061809-112742"},{"key":"e_1_3_2_4_2","doi-asserted-by":"publisher","DOI":"10.1128\/AAC.00226-09"},{"key":"e_1_3_2_5_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.jmb.2007.05.093"},{"key":"e_1_3_2_6_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.71.2.417"},{"key":"e_1_3_2_7_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.bmcl.2008.06.068"},{"key":"e_1_3_2_8_2","doi-asserted-by":"publisher","DOI":"10.1038\/nature05689"},{"key":"e_1_3_2_9_2","doi-asserted-by":"crossref","first-page":"139","DOI":"10.1093\/oxfordjournals.jbchem.a123853","article-title":"Reaction mechanism of glutamate racemase, a pyridoxal phosphate-independent amino acid racemase","volume":"112","author":"Choi SY","year":"1992","unstructured":"Choi SY, Esaki N, Yoshimura T, Soda K. 1992. 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